Haque, Md. Mamunul Kim, Dohee Yu, Young Hyun Lim, Sungsu Kim, Dong Jin Chang, Young-Tae Ha, Hyung-Ho Kim, Yun Kyung 2024-01-20T09:01:52Z 2024-01-20T09:01:52Z 2022-01-10 2014-09 1350-6129 https://pubs.kist.re.kr/handle/201004/126381 Abnormal tau aggregates are presumed to be neurotoxic and are an important therapeutic target for multiple neurodegenerative disorders including Alzheimer's disease. Growing evidence has shown that tau intermolecular disulfide cross-linking is critical in generating tau oligomers that serve as a building block for higher-order aggregates. Here we report that a small molecule inhibitor prevents tau aggregation by blocking the generation of disulfide cross-linked tau oligomers. Among the compounds tested, a rosamine derivative bearing mild thiol reactivity selectively labeled tau and effectively inhibited oligomerization and fibrillization processes in vitro. Our data suggest that controlling tau oxidation status could be a new therapeutic strategy for prevention of abnormal tau aggregation. English TAYLOR & FRANCIS LTD Inhibition of tau aggregation by a rosamine derivative that blocks tau intermolecular disulfide cross-linking Article 10.3109/13506129.2014.929103 1 Amyloid: The Journal of Protein Folding Disorders, v.21, no.3, pp.185 - 190 Amyloid: The Journal of Protein Folding Disorders 21 3 185 190 N scie scopus 000340428000006 2-s2.0-84906279142 Biochemistry & Molecular Biology Medicine, General & Internal Medicine, Research & Experimental Biochemistry & Molecular Biology General & Internal Medicine Research & Experimental Medicine Article PROTEIN-TAU IN-VITRO OLIGOMERS BETA(2)-MICROGLOBULIN NEURODEGENERATION PATHOLOGY TANGLES DOMAIN In-gel fluorescence intermolecular disulfide bond rosamine small molecule inhibitor Tau oligomerization thiol reactivity